ID A0A0L0GGX1_9ENTR Unreviewed; 541 AA.
AC A0A0L0GGX1;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Oxidoreductase {ECO:0000313|EMBL:KNC88257.1};
GN ORFNames=GM31_11070 {ECO:0000313|EMBL:KNC88257.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC88257.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC88257.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC88257.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(2015).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC88257.1}.
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DR EMBL; JNGI01000184; KNC88257.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0GGX1; -.
DR STRING; 379893.GCA_001297775_02505; -.
DR PATRIC; fig|379893.4.peg.2252; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000037393; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
DR PROSITE; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU003968};
KW Reference proteome {ECO:0000313|Proteomes:UP000037393}.
FT DOMAIN 102..125
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 279..293
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 112..115
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 244
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 468..469
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 541 AA; 59215 MW; 87B96EEF031CDCF1 CRC64;
MSVDSISKIG AADDHGSLTF GLKSNYDFIV CGAGSAGCVV AARLSELPGV QVLLLEAGDD
DVSPTISDPG SWPLNLGSKY DWNFVGEPNP HLNGRRLPLN MGKGLGGGSS INVMVWSRGH
KTDWDFFASE SGDSGWEYES ILGYYRRIEN WQGAPDQRRR GTGGPVYVAP AAEPQPLVHA
TLQAASAFGI PRFDSPNGEM MEGPGGVAIA DLRIRDGRRQ SLYRSYVYPR MYQPNLTVVT
HALVTRLLFE GKQVVGVEAV INGQLCRIGV LCEVILSMGA IQTPKVLMQS GIGPQHELRR
HGIEVVEHHP GVGQNHQDHI AFGCTWEYRT PQPINAGGCE STLYWKSDSR LDAPDLLQCQ
LEFAVPSPPE VGIDPPEHGW TMFAGLARPK SRGSLRLTGA NPDDPLLIDP NVLSEPEDLE
AAFATVELCR AIGNHLRFDN LIKREVTPLY RERREMEQFL RNSAVTFWHQ SCTAKMGRDA
MSVVDGQLRV YGIKNLRIAD ASIMPRIPVG NIMAPCVVIG ERAADLIKAT HGLQTMGSHY
F
//
